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1
Complex formation of guanidinated bovine trypsin inhibitor (Kunitz) with trypsin, chymotrypsin and trypsinogen as studied by the spin-label technique.
FEBS Lett. 1982 Apr 5;140(1):53-7. doi: 10.1016/0014-5793(82)80519-x.
2
High-level bacterial expression and 15N-alanine-labeling of bovine trypsin. Application to the study of trypsin-inhibitor complexes and trypsinogen activation by NMR spectroscopy.
Biochemistry. 2001 May 29;40(21):6275-83. doi: 10.1021/bi0100992.
3
Interaction of the Kunitz soybean trypsin inhibitor with bovine trypsin. Evidence for an an acy-enzyme intermediate during complexation.
Biochemistry. 1977 May 31;16(11):2474-8. doi: 10.1021/bi00630a024.
4
Pre-existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz).
FEBS Lett. 1976 Apr 1;63(2):240-4. doi: 10.1016/0014-5793(76)80103-2.
5
Binding of the bovine pancreatic secretory trypsin inhibitor (Kazal) to bovine serine (pro)enzymes.
J Mol Biol. 1987 Nov 5;198(1):129-32. doi: 10.1016/0022-2836(87)90463-3.
6
Spin-labeled sulfonyl fluorides as active site probes of protease structure. I. Comparison of the active site environments in alpha-chymotrypsin and trypsin.
J Biol Chem. 1974 Mar 25;249(6):1668-77.
7
Interaction between serine (pro)enzymes, and Kazal and Kunitz inhibitors.
J Mol Biol. 1983 Apr 15;165(3):543-58. doi: 10.1016/s0022-2836(83)80219-8.
8
Soybean trypsin inhibitor (Kunitz) is doubleheaded. Kinetics of the interaction of alpha-chymotrypsin with each side.
Biochim Biophys Acta. 1981 Jan 15;657(1):58-72. doi: 10.1016/0005-2744(81)90130-3.
9
Effect of serum alpha2-macroglobulin on the trypsin-soybean trypsin inhibitor complex.
Arch Roum Pathol Exp Microbiol. 1974 Jul-Dec;33(3-4):325-33.
10
A study of the active center of trypsinogen by comparative affinity chromatography of trypsinogen, alpha-, beta-, psi-trypsins, DIP-trypsin, chymotrypsinogen, alpha-chymotrypsin and elastase.
Int J Pept Protein Res. 1974;6(1):37-41. doi: 10.1111/j.1399-3011.1974.tb02356.x.
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